ID A0A2S6C3H0_9PEZI Unreviewed; 760 AA. AC A0A2S6C3H0; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 19-JAN-2022, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PPJ54246.1}; GN ORFNames=CBER1_05123 {ECO:0000313|EMBL:PPJ54246.1}; OS Cercospora berteroae. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora. OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ54246.1, ECO:0000313|Proteomes:UP000237631}; RN [1] {ECO:0000313|Proteomes:UP000237631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631}; RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C., RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A., RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.; RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic RT mechanisms and extends production to the genus Colletotrichum."; RL bioRxiv 0:0-0(2017). CC -!- SIMILARITY: Belongs to the TMCO4 family. CC {ECO:0000256|ARBA:ARBA00009824}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PPJ54246.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PNEN01000569; PPJ54246.1; -; Genomic_DNA. DR STRING; 357750.A0A2S6C3H0; -. DR Proteomes; UP000237631; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR007941; DUF726. DR PANTHER; PTHR17920; PTHR17920; 1. DR Pfam; PF05277; DUF726; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000237631}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294..317 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 337..355 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 83..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 150..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 653..682 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 709..760 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 266..287 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 150..178 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 709..753 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 760 AA; 83524 MW; 8E6E6D1DF0FF2414 CRC64; MFNKISTPFS NRANGGAGEE EAQGETLTTI LSTHEDRTAL TLLIADCTEA MKQNIEDAFD ATQTGSNTSL VVEDLREALP DVDAEASDEK VQSETEDAVQ KQKELEKEQK ELAQREKELA EAKSKELKSA ALEHWDKWRS SVIQRVGEVL NSHEEEERRQ KRESESSKKK EEEARAASPP MRFESPPKYD KAVDDSMRAL YPPIDCPLRR LTEEQRTLIL HCLLLLLLSL EHYHAESRIL LLRLSTSLDL PIDVLGLDES KVARGLLAAA ENMTADEETK KKAEENKTAR RWKVGLATAA GAALIGVTGG LAAPLLAAGV GTVMGGIGLA GTATAGYLGA LAGSGVLVGG LFGAYGGRMT GKMMDEYAKE IEDFGFEPVR TRHRPRKIEK EFRRLRVAIG ISGWLTKQEE VVEPWKVIGV QLESFALRWE LEALMNLGNS ISTFVTSTAW AYAKTEIIKR TLLGALYAGL WPLALLKVGR IIDNPFSVAN HRAQKCGEVL ADALINKAQG ERPVTLIGYS MGAKVVYACL QQLAERKAFG LVENAILIGT PASATSAEWR NLRAVVSGRL VNIYSTNDYV LGYLYRSQSI SLGVAGLQAI EHVKGVENFD VSSLVNGHTR YRFLTGPILQ QIGFEDVDLE GLKEEEVGLK ELDEKENRER AENEEKEKAK GSSSKEVSDE YVQGLEKEVE KKNEQSYIGW AQSKMVSAGS SVSAAYDKAT AQWRQRTKKN DSAMAGTGTP NVQTKSTEEQ PPALPQRPAQ //